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Pellino1 specifically binds to phospho-Thr18 of p53 and is recruited to sites of DNA damage.
Dai, Liang; Lin, Jianqing; Said, Aminahtusaidah Binte; Yau, Yin Hoe; Shochat, Susana Geifman; Ruiz-Carrillo, David; Sun, Kang; Chandrasekaran, Ramya; Sze, Siu Kwan; Lescar, Julien; Cheung, Peter Cf.
Afiliação
  • Dai L; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Lin J; School of Biological Sciences, Nanyang Technological University, Singapore; Nanyang Institute of Structural Biology, Nanyang Technological University, Singapore.
  • Said AB; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Yau YH; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Shochat SG; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Ruiz-Carrillo D; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Sun K; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Chandrasekaran R; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Sze SK; School of Biological Sciences, Nanyang Technological University, Singapore.
  • Lescar J; School of Biological Sciences, Nanyang Technological University, Singapore; Nanyang Institute of Structural Biology, Nanyang Technological University, Singapore. Electronic address: julien@ntu.edu.sg.
  • Cheung PC; School of Biological Sciences, Nanyang Technological University, Singapore. Electronic address: pcfcheung@ntu.edu.sg.
Biochem Biophys Res Commun ; 513(3): 714-720, 2019 06 04.
Article em En | MEDLINE | ID: mdl-30987826
Pellino1 is an E3 ubiquitin ligase that plays a key role in positive regulation of innate immunity signaling, specifically required for the production of interferon when induced by viral double-stranded RNA. We report the identification of the tumor suppressor protein, p53, as a binding partner of Pellino1. Their interaction has a Kd of 42 ±â€¯2 µM and requires phosphorylation of Thr18 within p53 and association with the forkhead-associated (FHA) domain of Pellino1. We employed laser micro-irradiation and live cell microscopy to show that Pellino1 is recruited to newly occurring DNA damage sites, via its FHA domain. Mutation of a hitherto unidentified nuclear localization signal within the N-terminus of Pellino1 led to its exclusion from the nucleus. This study provides evidence that Pellino1 translocates to damaged DNA in the nucleus and has a functional role in p53 signaling and the DNA damage response.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dano ao DNA / Proteínas Nucleares / Proteína Supressora de Tumor p53 / Ubiquitina-Proteína Ligases Limite: Humans Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Singapura

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dano ao DNA / Proteínas Nucleares / Proteína Supressora de Tumor p53 / Ubiquitina-Proteína Ligases Limite: Humans Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Singapura